AT1A2_CHICK
ID AT1A2_CHICK Reviewed; 1017 AA.
AC P24797;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-2;
DE Short=Na(+)/K(+) ATPase alpha-2 subunit;
DE EC=7.2.2.13;
DE AltName: Full=Sodium pump subunit alpha-2;
GN Name=ATP1A2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2171348; DOI=10.1152/ajpcell.1990.259.4.c619;
RA Takeyasu K., Lemas V., Fambrough D.M.;
RT "Stability of Na(+)-K(+)-ATPase alpha-subunit isoforms in evolution.";
RL Am. J. Physiol. 259:C619-C630(1990).
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.13;
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; M59959; AAA48981.1; -; mRNA.
DR PIR; I50394; A37227.
DR RefSeq; NP_990807.1; NM_205476.1.
DR AlphaFoldDB; P24797; -.
DR SMR; P24797; -.
DR PRIDE; P24797; -.
DR GeneID; 396468; -.
DR CTD; 477; -.
DR VEuPathDB; HostDB:geneid_396530; -.
DR InParanoid; P24797; -.
DR OrthoDB; 388324at2759; -.
DR PhylomeDB; P24797; -.
DR PRO; PR:P24797; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; ISS:UniProtKB.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0001504; P:neurotransmitter uptake; ISS:AgBase.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0006942; P:regulation of striated muscle contraction; ISS:AgBase.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Sodium; Sodium transport;
KW Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1017
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 2"
FT /id="PRO_0000046297"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..786
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 787..796
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 818..837
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 838..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 861..912
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..932
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 933..945
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 946..964
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 965..979
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1001..1017
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..79
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT REGION 207..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 371
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 711
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 937
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1017 AA; 112051 MW; 38E87C1BDE93B8C5 CRC64;
MDGREYSPAA TTSENGGGRR KQKEKELDEL KKEVNLDDHK LSLDELGRKY QVDLSRGLSN
ARAAEVLAQD GPNALTPPPT TPEWVKFCRQ LFGGFSILLW IGAILCFLAY GIQAAMEDEP
SNDNLYLGVV LAAVVIVTGC FSYYQEAKSS KIMDSFKNMV PQQALVIREG EKIQINAENV
VVGDLVEVKG GDRVPADMRI ISSHGCKVDN SSLTGESEPQ TRSPEFTHEN PLETRNICFF
STNCVEGTAR GIVISTGDRT VMGRIASLAS GLEVGRTPIA MEIEHFIRLI TGVAVFLGLS
FFILSLILGY TWLEAVIFLI GIIVANVPEG LLATVTVCLT LTAKRMARKN CLVKNLEAVE
TLGSTSTICS DKTGTLTQNR MTVAHMWFDN QIHEADTTED QSGATFDKRS PTWAALSRIA
GLCNRAVFKP GQENISISKR DTAGDASESA LLKCIQLSCG SVKKMRDKNP KVTEIPFNST
NKYQLSIHER EEDPQGHILV MKGAPERILE RCSRILLQGQ EVPLDEEMKE AFQNAYLELG
GLGERVLGFC HLYLPPDKFP RGFRFDADEV NFPTSDLCFV GLMSMIDPPR AAVPDAVGKC
RSAGIKVIMV TGDHPITAKA IAKGVGIISE GNETVEDIAA RLNIPVSQVN PREAKACVVH
GSDLKDMTAE QLDEILRNHT EIVFARTSPQ QKLIIVEGCQ RQGAIVAVTG DGVNDSPALK
KADIGIAMGI AGSDVSKQAA DMILLDDNFA SIVTGVEEGR LIFDNLKKSI AYTLTSNIPE
ITPFLLFIIA NIPLPLGTVT ILCIDLGTDM VPAISLAYEA AESDIMKRQP RNPRTDKLVN
ERLISMAYGQ IGMIQALGGF FTYFVILAEN GFLPARLLGV RLAWDDRSTN DLEDSYGQEW
TYEQRKVVEF TCHTAFFASI VVVQWADLII CKTRRNSVFQ QGMKNKILIF GLLEETALAA
FLSYCPGMGV ALRMYPLKVT WWFCAFPYSL LIFAYDEVRK LILRRYPGGW VEKETYY
